Dergiler / Turkish Journal of Biology / 2014 / Cilt: 38 - Sayı: 4

Characterization of dehydrin AhDHN from Mediterranean saltbush (Atriplex halimus)

Sayfa
469–477
Yayın Tarihi
2014-04-01
DOI
—
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

The novel AhDHN gene can be potentially utilized in transformation of other plants to improve tolerance to salinity stress.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez:Dehydrins are a group of proteins whose expression is associated with plant abiotic stresses and seed maturation.
📊
Temel Bulgular & Veri:The AhDHN amino acid sequence revealed 1 S-segment, 3 K-segments (K1, K2, K3), and a transmembrane pore-lining signature.
💡
Sonuç & Katkı:The novel AhDHN gene can be potentially utilized in transformation of other plants to improve tolerance to salinity stress.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Atriplex halimus · dehydrin · expression

Özet

Dehydrins are a group of proteins whose expression is associated with plant abiotic stresses and seed maturation. The full AhDHN dehydrin gene from Mediterranean saltbush (Atriplex halimus) was cloned and characterized. The AhDHN amino acid sequence revealed 1 S-segment, 3 K-segments (K1, K2, K3), and a transmembrane pore-lining signature. It is a 26.77-kDa protein with a predicted isoelectric point of 6.14. Phylogenetic analysis of the AhDHN protein clustered it with other proteins from related plants belonging to the family Amaranthaceae (Atriplex canescens, Spinacia oleracea, Suaeda salsa, and Suaeda glauca). The AhDHN protein sequence revealed a deletion that was 102 amino acids long compared to AcDHN from A. canescens. The expression level of the AhDHN gene was found to be enhanced by salinity stress in Mediterranean saltbush roots but not in shoots. The novel AhDHN gene can be potentially utilized in transformation of other plants to improve tolerance to salinity stress.

Abstract

Dehydrins are a group of proteins whose expression is associated with plant abiotic stresses and seed maturation. The full AhDHN dehydrin gene from Mediterranean saltbush (Atriplex halimus) was cloned and characterized. The AhDHN amino acid sequence revealed 1 S-segment, 3 K-segments (K1, K2, K3), and a transmembrane pore-lining signature. It is a 26.77-kDa protein with a predicted isoelectric point of 6.14. Phylogenetic analysis of the AhDHN protein clustered it with other proteins from related plants belonging to the family Amaranthaceae (Atriplex canescens, Spinacia oleracea, Suaeda salsa, and Suaeda glauca). The AhDHN protein sequence revealed a deletion that was 102 amino acids long compared to AcDHN from A. canescens. The expression level of the AhDHN gene was found to be enhanced by salinity stress in Mediterranean saltbush roots but not in shoots. The novel AhDHN gene can be potentially utilized in transformation of other plants to improve tolerance to salinity stress.

🔖

Bu Makaleye Atıf Yap

SADDER, M. T., AL-DOSS, A. A. (2014). Characterization of dehydrin AhDHN from Mediterranean saltbush (Atriplex halimus). Turkish Journal of Biology, Cilt: 38 - Sayı: 4, 469–477. https://ajindex.com/articles/181742

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (13)

  1. Al-Turki TA, Omar S, Ghafoor A (2000). A synopsis of the genus Atriplex L. (Chenopodiaceae) in Saudi Arabia. Feddes Repert 111: 261–293.
  2. Archambault A, Strömvik MV (2012). The Y-segment of novel cold dehydrin genes is conserved and codons in the PR-10 genes are under positive selection in Oxytropis (Fabaceae) from contrasting climates. Mol Genet Genomics 287: 123–142.
  3. Ayarpadikannan S, Chung E, Cho CW, So HA, Kim SO, Jeon JM, Kwak MH, Lee SW, Lee JH (2012). Exploration for the salt stress tolerance genes from a salt-treated halophyte, Suaeda asparagoides. Plant Cell Rep 31: 35–48.
  4. Borovskii GB, Stupnikova IV, Antipina AI, Vladimirova SV, Voinikov VK (2002). Accumulation of dehydrin-like proteins in the mitochondria of cereals in response to cold, freezing, drought and ABA treatment. BMC Plant Biol 2: 5. Buchan DW, Ward SM, Lobley AE, Nugent TC, Bryson K, Jones DT (2010). Protein annotation and modelling servers at University College London. Nucleic Acids Res 38: W563–W568. Carjuzaa P, Castellión M, Distéfano AJ, del Vas M, Maldonado S (2008). Detection and subcellular localization of dehydrin-like proteins in quinoa (Chenopodium quinoa Willd.) embryos. Protoplasma 233: 149–156.
  5. Chen K, Fessehaie A, Arora R (2012). Dehydrin metabolism is altered during seed osmopriming and subsequent germination under chilling and desiccation in Spinacia oleracea L. cv. Bloomsdale: possible role in stress tolerance. Plant Sci 183: 27–36.
  6. Close TJ (1996). Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plantarum 97: 795–803.
  7. Danyluk J, Perron A, Houde M, Limin A, Fowler B, Benhamou N, Sarhan F (1998). Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat. Plant Cell 10: 623–638.
  8. Demirkaya M (2014). Improvement in tolerance to salt stress during tomato cultivation. Turk J Biol 38: 193–199.
  9. Felsenstein J (1989). PHYLIP - Phylogeny Inference Package (Version 3.2). Cladistics 5: 164–166.
  10. Glenn EP, Brown JJ, Blumwald E (1999). Salt tolerance and crop potential of halophytes. Crit Rev Plant Sci 18: 227–255.
  11. Hall TA (1999). BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/ NT. Nucl Acid S 41: 95–98.
  12. Hanin M, Brini F, Ebel C, Toda Y, Takeda S, Masmoudi K (2011). Plant dehydrins and stress tolerance: versatile proteins for complex mechanisms. Plant Signal Behav 6: 1503–1509.
  13. Hara M, Kondo M, Kato T (2013). A KS-type dehydrin and its re